JPH02131537A - Preparation of cheese food - Google Patents

Abstract

PURPOSE:To prepare an easily meltable cheese food having stringiness and high-temperature shape-retainability and exhibiting excellent chewability, etc., by adding a meltable salt to a cheese and reacting the resultant molten cheese having a specific composition with a transglutaminase. CONSTITUTION:Water and a meltable salt (e.g., citric acid) and, as necessary, seasonings, flavors, milk-originated proteins, etc., are added to natural cheese or process cheese, and the mixture is melted to obtain a molten cheese having a milk solid content of >=35wt.% and a milk protein content of >=13wt.%. An aqueous solution of a transglutaminase is added to the molten cheese and uniformly dispersed to effect enzymatic reaction. After the simultaneous inactivation of the enzyme and sterilization of the reaction mixture, the mixture is optionally filled in a container and allowed to cool to obtain the objective cheese food. The transglutaminase used in the above process is e.g., the one separated from the liver of guinea pig, produced by microorganisms, etc.

Description

Detailed Description of the Invention <<Industrial Application Fields> The present invention uses natural cheese or processed cheese as the main raw material, and contains water, molten salt, and optionally various additives, such as milk-derived proteins, seasonings, and A cheese melted product prepared by melting and preparing a flavoring agent is treated with transglutaminase, and has a suitable combination of melting deformability (easy meltability) and stringiness by heating, or does not cause melting deformation by heating. (Heat-resistant shape retention) A method for producing a cheese food having a texture similar to Kamaboni 1 with good crispness.

(Prior art and problems) Most of the processed cheeses produced by conventional methods have protein converted to sodium chloride and sodium chloride, so they do not melt even when heated in an oven, etc., and have moderate fluidity. It has the disadvantage that it is unsuitable for applications that require high quality (such as hamburgers and pizza pies).Also, natural cheese is unsuitable for the above applications because it deforms and melts excessively due to heat. In recent years, research has been conducted on easily melted processed cheeses, but even though the melting properties have been improved, they usually do not have stringiness, and it is difficult to carry out bleaching studies on cheeses. In this case, the unique cheese odor of cheese or its stickiness when eaten is one of the reasons for low preference for cheese, and this has resulted in hindering the expansion of cheese consumption.

In addition, in recent years, cheese has been used in fish paste products, hamburgers, and various other prepared foods to improve their stickiness and flavor. However, the cheese in this case generally tends to deform and melt due to heat. Therefore, depending on the product form, it could not be said that the product had high commercial value. Furthermore, even those that cannot be melted by heat have an adhesive texture and tend to adhere to teeth.

(Problems to be Solved by the Invention) The present invention attempts to solve the above-mentioned problems, and provides a cheese food that has both melt deformability and stringiness when heated, and a cheese food that has heat-resistant shape retention and texture. It is an object of the present invention to provide a method for producing a crispy cheese food that is different from conventional cheese-like structures, and a cheese food produced in this manner.

(Means for solving and overcoming problems, effects of the invention) The present invention has the following features:
A melted cheese made from natural cheese or processed cheese as the main raw material, water, molten salt, and optionally various additives is heated and sterilized as necessary.
When producing cheese food by cooling, if transglutaminase (hereinafter sometimes abbreviated as TGaSe) is applied to the melted cheese, the properties of the cheese food obtained can be changed under the action conditions. It was discovered that the desired meltability and stringiness can be easily imparted to the hood at the same time, or the desired heat-resistant shape retention properties can be easily imparted to the hood, and the invention was completed based on this knowledge.

Incidentally, there has never been an example of using TGaSe when manufacturing a cheese food using natural cheese or processed cheese as the main raw material.

In the present invention, easy meltability refers to the property of relatively easily melting (meltdown) when heated using an oven, etc., and stringability refers to the property of making the yarn melt when heated using an oven etc. The property of pulling and heat-resistant shape retention is the property of maintaining the same shape without melting (meltdown) when heated using an oven or the like.

The method of the present invention will be explained in detail below.

As mentioned above, the properties of the resulting cheese food can be changed by changing the conditions under which TGase acts, but generally speaking, if you make TGaSe act more mildly, such as by making it act in a smaller amount and for a shorter time, A cheese food that has both easy meltability and stringiness can be obtained, while a cheese food that has excellent heat resistance and shape retention can be obtained by acting more strongly.

TGase for imparting desired properties to cheese foods
The specific operating conditions for can be determined very easily by those skilled in the art by conducting preliminary experiments in consideration of what will be explained below.

As the raw material cheese used in the present invention, a wide variety of cheeses can be used, and from unripe to highly matured cheeses, for example, natural cheeses such as Gogue cheese and cheddar cheese, and processed cheeses can be used.

Molten salts such as various phosphorous salts and citric acid can be used alone or in combination of two or more, as in the case of manufacturing cheese food using well-known natural cheese and processed cheese as the main ingredients. be.

Various additives that may be added as desired include milk-derived protein, seasonings, fragrances, etc., which are the same as in the case of producing cheese food by conventional methods.

Raw cheese, molten salt, various optional additives, and water are placed in, for example, an emulsifiable container and mixed.

The molten salt is 1 to 3% by weight per 1 part by weight of the raw material.
Preferably 2 to 2.5% by weight is used.

If too little salting is used, it will result in poor emulsification and a hard structure, and if it is too much, it will become a source of soft tissue and chemical odor originating from molten salt. Various additives are the same as in the conventional method,
This is normally within 1/6 of the solid content of the product when food is added for the purpose of imparting aroma and taste, and within 10% of the weight of the final product for each component not derived from milk.

The raw cheese and added water differ slightly depending on the characteristics desired to be imparted to the cheese food. When it is desired to impart meltability and stringiness by heating, melted cheese should have a milk solids content of 3%.
The raw material cheese is selected so that the milk protein content is 13 times or more, preferably 13 to 20 times, and the amount of added water is selected so that the milk protein content is 5 times ω% or more, preferably 35 to 40 times ω%. If the milk solid content and milk protein content are outside the above ranges, meltability and stringiness will not be exhibited upon heating.

When heat-resistant retention is desired, the milk solid content in the cheese@lysed product is 401 td% or more, preferably 40 to 45 wt r%, and the milk protein color is 15 wt w% or more, preferably 15 to 45 wt%.
Select raw materials and add water so that the amount is 20j4 ffi%. If the milk solid content and milk protein content are outside the above ranges, proper heat resistance and shape retention will not be achieved, resulting in a poorly defined structure.

Next, the mixture is heated to, for example, 85° C. by heating the container with hot water, and stirred and emulsified to obtain a melted cheese in which the cheese is completely melted.

To allow transglutaminase to act on melted cheese, proceed as follows.

The transglutaminase used in the present invention is irrespective of its origin; for example, it may be isolated from the liver of a guinea pig (hereinafter sometimes abbreviated as MTGase), or it may be produced by microorganisms, and hereinafter abbreviated as BTGase. There is. The former MTGaSe is
For example, it can be prepared by the method described in JP-A-58-14964. The latter, BTGase, is a novel enzyme, an invention in which some of the present inventors were involved as inventors (
The enzyme properties, manufacturing method, etc. are described in a separate section.

The amount of l''Qase to be used varies depending on the properties desired to be imparted to the cheese. When it is desired to impart meltability and stringability upon heating, the amount is 5 to 20 U1, preferably 8 to 13 U, per 1 g of protein in the melted cheese.

If TGaSe is used for too little time, the stringiness will deteriorate and the tissue will become soft. If the amount increases, desired easy solubility and stringiness cannot be obtained, and heat-resistant shape retention properties will occur. When you want to impart heat-resistant shape retention, it is 12u or more, preferably 13u.
~15u. If TGase is used too much, the resulting tissue will be very hard and poorly articulated, leaving lumps in the oral cavity.

For example, dissolve TGase in a small amount of water and use it as described above.
Mix and disperse evenly into the melted Mengki cheese. TGase
If TGase is dependent on a specific substance, as is the case with TGase, that substance can of course coexist with TGase.

When mixing for 1 minute, take into consideration the operating temperature of TGase.
The temperature of the cheese melt is 40-60°C, preferably 45-60°C
The temperature is lowered in advance to 50°C, for example, 50°C.

The melted cheese in which TGase is uniformly dispersed and mixed is quickly filled and molded into a container as required, and maintained at the above temperature with hot water, for example, to allow TGase to act. The enzyme reaction time varies depending on the desired characteristics of the cheese food, and is 20 to 120 minutes if you want to give it meltability and stringiness by heating, preferably 25 to 60 minutes, and 1 to 60 minutes if you want heat-resistant shape retention. The duration is at least 1 hour, preferably 1 to 3 hours.

The cheese melt treated with TGaSe as described above is then sterilized by simultaneously deactivating the enzyme.

For example, using boiling water,
This can be done by holding for 0 minutes.

If necessary, the sterilized product is filled into a container and molded, and then cooled, for example, using a cold water cypress or a refrigerator, to produce a cheese food product.

Among the products obtained in this way, cheese food that has both meltability and stringiness when heated exhibits good meltdown properties (easy meltability) when heated, and has very smooth stringiness. It exhibits the following.

Furthermore, it has better crispness when chewing than ordinary natural cheese or processed cheese in the warmest state, and also has the property of being less likely to adhere to the inside of the oral cavity. Moreover, by seasoning, it is possible to provide products with a variety of tastes.

On the other hand, cheese food with heat-resistant shape retention f1 of 1-1'5 has good shape retention against heating and is a coagulated product that utilizes 1-lance glutaminose, so it is different from conventional cheese structures. It has a bamboo quality with good crispness. In addition, the above-mentioned equipment II v & is similar to [Kamabo] which is made mainly from fish protein, but it has 100% calcium and lower sodium than Kamabolo, and It is a high-energy product that contains a large amount of vitamin A. reactor. Furthermore, in the present invention, by seasoning? Providing products with a wide variety of tastes is also part of the town's Noh.

(1) Regarding the spinnability of cheese food, it is important to note that products containing a large amount of milk protein have low spinnability. The temperature range (stringing temperature range) tends to be on the high temperature side, and if the components are the same,
It has been found that the temperature range in which stringiness is exhibited also increases when a large amount of enzyme is added. In other words, when the enzyme activity is varied by adjusting the components, low activity results in the high 1 range, and high activity results in the low temperature range. On the other hand, when the enzyme activity is varied by adding the enzyme, the temperature range in which good stringiness is exhibited changes, such as a low temperature range when the activity is low and a high temperature range when the activity is high. The reaction bar is also a factor that should be kept in mind as it is one of the factors that affects stringiness. As mentioned above, the present invention was carried out in order to establish conditions that allow transglutaminase to act effectively, with the aim of achieving good meltdown properties and stringiness. It becomes a string-like substance that has strong properties and does not cause oil separation.

<<Novel Transglutaminase BTGase> (1) Transglutaminase and its Derivatives Transglutaminase (TGase) is a first-order acyl transfer reaction of the remaining γ to carpoxyamide group of glutamine in the peptide chain. This TG a se is an acidic receptor a {tree, and when the ε-7 mino V of the glutinous residue in the protein is produced, the ε-(γ-Qlu
) Lys crosslinks are formed. Furthermore, when water functions as a 7-syl receptor, it is an enzyme that proceeds with the reaction in which the remaining glutamine is deamidated to become a glutamic acid residue.

These properties of TGase allow it to be used to gel protein-containing solutions or slurries.

TGaSe has so far had seven moles! ~Liver-derived (M
Although animal-derived substances such as TGase) are known,
Those derived from original products are difficult to obtain at low cost and in human f'Q, and when gelling proteins, it is necessary to increase the enzyme ci degree and substrate concentration to J(, and Ca
Since it is 2° dependent, its uses are limited.

Novel transglutaminase (B) that can be used in the present invention
TGase) is produced by microorganisms, for example, bacteria of the genus Strebtoverticillium, but there are currently no reports on TGase derived from microorganisms.

BTGase derived from microorganisms that can be used in the present invention is available at low cost and is easily purified, so it is highly practical. In addition, by using BTGase, the enzyme (BTG
There is an advantage that a gelled product of excellent quality can be produced at a very low degree of ace)m and a very low substrate concentration.

■BTGase (7) [i The microorganism that produces BTGase is, for example, Streptoverticillium griseokanoreneum
ptoverticillm griseocar
neui) I F 012776, Streptoverticillium cinamoneum sub SB cinamoneum (3 treptoverticillium ci
nnamoncum sub sp. cinnaa+
oneum) IFO 12852, Streptoverticillium mobalaens
rt ic i l l iummobaraense
) I F Q 13819 etc.

The cultivation method, purification method, etc. for culturing these microorganisms and obtaining transglutaminase are as follows.

Although both liquid culture and solid culture are possible as culture formats, it is advantageous industrially to perform deep aeration agitation culture. In addition, the culture sources used include carbon sources, nitrogen sources, inorganic salts, and other microorganisms commonly used for microbial culture.
In addition to nutrient sources, any nutrient source that can be used by microorganisms belonging to the genus Strebtoverticillium can be used. Carbon sources for the culture medium include glucose, sucrose, lastagen, glycerin, dextrin, starch, etc., as well as fatty acids, fats and oils,
Existing Bill etc. may be used alone or in combination. As the nitrogen source, either an inorganic nitrogen source or an organic nitrogen source can be used, and examples of the inorganic nitrogen source include ammonium nitrate, ammonium sulfate, urea, sodium nitrate, and ammonium chloride. Examples of organic nitrogen sources include flour, bran, and defatted lees of soybeans, rice, corn, and wheat, as well as cornstarch liquor, vegetable oil, meat extract, casein, amino acids, and N mother extract. Salt-free and slightly salt-free
! Nutrients A include salts such as phosphoric acid, magnesium, potassium, iron, calcium, and zinc, as well as vitamins, nonionic surfactants, and antifoaming agents that promote bacterial growth and the production of King B GaSe. It can be used as needed.

PJ cultivation is cultivated under aerobic conditions! At M temperature, bacteria grow [3T
It may be within the range that Gase is produced, preferably 2
The temperature is 5-35°C. Cultivation time varies depending on conditions, but
It is sufficient to culture until the time when BTGase is produced the most, which is usually about 2 to 4 days.

In liquid culture, BTGase is dissolved in the culture solution, and after the completion of culture, it is collected from the culture filtrate after removing the solid content from the culture solution.

To purify BTGaSe from culture filtrate, any method commonly used for enzyme purification can be used.

For example, treatment with organic solvents such as ethanol, acetone, and isobrobyl alcohol, salting out with ammonium sulfate, salt, etc.
Methods such as dialysis, ultrafiltration, ion exchange chromatography, adsorption chromatography, gel filtration, adsorbents, and isoelectric point fractionation can be used. In addition, by appropriately combining these methods, if the degree of purification of BTGase is 12, it is possible to perform the method in an appropriate combination. Enzymes obtained by these methods are stabilized by various salts, sugars, proteins,
Liquid or solid BTGase can be obtained by ultrafiltration concentration, reverse osmosis concentration, vacuum drying, freeze drying, and spray drying, with or without adding lipids, surfactants, etc.

[Activity measurement of 3TGase was performed using pendyloxycarbonyl-glutaminylglycine and hydroxylamine.
As a quality, the reaction is carried out in the presence of Ca2+8, the produced hydroxamic acid is formed into an iron complex in the presence of tricloacetic acid, the absorption at 525 nm is measured, and the activity is determined by determining the suspension of hydroxamic acid from the detection line.

BTGase activity was measured by the method described below unless otherwise specified.

Activity measurement method> Reagent A 0.2M Tris-HCl buffer (pH 6.010.
1M hydroxylamine 0. OiMN archetype glutathione A 003M penzyloxynonorbonyl-1-glutaminylglycine reagent 8 3N-hydrochloric acid 12% monotrichloroacetic acid 5% FeCI ・ f3 To 1 2
0 (Dissolved in 0.INHCρ) A 1:1:1 mixture of the above solutions was used as Sample B.

Add 0.5d of reagent A to enzyme solution 005d and mix 3.
After reacting at 7°C for 10 minutes, test [8] was added to stop the reaction and Fe
Measure the absorbance at 9525 nm at which the inscription was formed. As a control, the absorbance of a similarly reacted enzyme solution that has been heat-inactivated in advance is measured, and the difference in absorbance from the solution is determined. Separately, a hanging line was prepared using 1-glutamic acid γ-monohydroxamic acid instead of the enzyme solution, and a of the generated hydroxamic acid was determined from the difference in absorbance of the pre-distribution.
The enzyme activity that produced 1 μmol of hydroxamic acid per minute was designated as position 1131.

GBTGase (7) gi properties Purified BTGase ISed as above, i.e. transglutaminase of Streptobedicillium mobans IF01381g (named BTG-1), Streptobedicillium griseoluneum IF O
12776 1-transglutaminase (named BTG-2), Strebtoverdicillium cinnamoneum sub-SB cinnamoneum IF 0 Enzyme chemical properties of 12852 transglutaminase (named BTG-3) is as follows.

a) Optimum pH: 37 when penzyloxycarbonyl-glutaminylglycine and hydroxylamine are used as substrates.
The optimal pl-1 of BTG-1 is 6-7 in a 10-minute reaction at °C.
The optimum 11H of BTG-2 is around 6-1,
The optimum ρH of BTG-3 is around 6 to γ.

b) Optimal temperature: When pendynoleoxycanolebonyl-glutaminylglycine and hydroxylamine are used as substrates,
ilH6, 10 minute reaction, the optimum temperature of 87G-1 is 5
The optimal temperature for BTG-2 is around 45°C, and the optimal temperature for BTG-3 is around 45°C.

c) pH stability: After treatment at 37°C for 10 minutes, BTG-1 had r)H 5~
BTG-2 is stable at DH 5-9 and BTG-3 is stable at l)H 6-9.

d) Temperature stability: After treatment with pl-17 for 10 minutes, BTG-1 had 88% activity remaining at 40°C, γ4% activity remained at 50°C, and BTG-2 had 86% activity remaining at 40°C. Remains at 50℃
56% activity remains, and BTG-3 remains 80% at 40°C.
Activity remains, with 53% activity remaining at 50°C.

0) Substrate specificity: Using each BTGase, reactions between various synthetic substrates and hydroxylamine were investigated. None of the BTGases reacts when the synthetic substance is penzyloxycarbonyl asparaginylglycine, penzyloxycarbonylglutamine, or glycylglutaminylglycine. However, the reactivity is highest when the synthetic substrate is penzyloxyglutaminylglycine. At this time, the degree of various synthetic substrates was 5
mH. The Song Dynasty is shown in Table-1.

In addition, CBZ in Table 1 is an abbreviation for penzyloxycarbonyl group, Qln is a glutaminyl group, and G1
y stands for glycyl group, ASρ is asparaginyl L
It is an abbreviation of t.

Table-1 f) Metal ion Akira v! : Various metal ions were added to the activity measurement system at a concentration of 1 mM to examine their effects (results are shown in Table 2).

The activity of any BTGase is inhibited by Cu2+7n2'.

Table g) Inhibitor effects: Each inhibitor was added to 1 mM and the activity was measured at 25°C for 30 minutes.The results are shown in Table 3).

Both BTGases include rose chloromercury benzoin M (abbreviated as PCMB), N-edylmaleimide (NE
(abbreviated as M), the activity of which is inhibited by monoiodoacetic acid.

Table 3 In Table 3, PMSF is an abbreviation for phenylmethylsulfonyl fluoride.

h) Isoelectric point: As determined by ampholine isoelectric focusing, BT
The isoelectric point 1) I of G-1 is around 9, the isoelectric point pi of BTG-2 is around 9.7, and the isoelectric point pl of BTG3 is around 9.8.

) Molecular suspension: As determined by SOS disk electrophoresis, BTG-
The molecular weight of BTG-1 is approximately 38,000, the molecular weight of BTG-2 is approximately 41,000, and the molecular weight of BTG-3 is approximately 41,000.

j) Comparison with MTGase: Next, the properties of BTGase and guinea pig liver-derived transglutaminase (MTGase) will be compared. Furthermore, M
TGase was prepared by the method described in JP-A-58-149645.

Table 4 shows a comparison of the chemical properties of each enzyme, and Table 5 shows Ca
The effect on the activity of 2+ is shown. As is clear from Tables 4 and 5, MTGa, which has been mainly studied in the past,
There are various differences in enzymatic chemical properties between se and BTGase derived from actinomycetes, especially temperature stability, molecular; f
Differences are seen in H, isoelectricity, and group^1 specificity. Also, C
BTGase is clearly different from MTGase in that it can act in the presence and absence of a2+. Follow T. , each enzyme of BTGase is M T G a
It is thought that its properties are different from Se.

Table-5 Table (4) 8 TG asa's "IJ 'lb }
5'1a) Production of H'rG-1 Strebtoberb-silium [Baraience IF0 1
3819 in a medium containing 0.2% polybebutone, 0.5% glycose, 0.2% dipotassium phosphate, and 0.1% magnesium sulfate (1) H7) 200〃ii!
Inoculated into a tube, cultured at 30°C for 48 hours, and then
g nutrient solution containing 2.0% polybebutone, 20% lastagen,
Dipotassium phosphate 02%, magnesium sulfate 0.1%,
Medium 201' (1) consisting of 02% yeast extract and 005% antifoaming agent Aγcanol (trade name, Asahi Denka product)
H7) was cultured at 30°C for 3 days, and the culture solution 18
I got 5l. The activity of this product is 0. 35u/+j! It is.

Adjust the culture medium to 1) 6.5 with hydrochloric acid and set it to 0. 05
It was passed through a column of CG-50 (trade name, manufactured by Organo Inc.) which had been equilibrated with M non-acid buffer (t)Hl 3.5).

With this procedure, the transglutamine was adsorbed.

Furthermore, after washing away impure proteins with the same buffer solution,
A concentration gradient of the same buffer solution of 0.05 to 0.5 M was prepared, and the eluate was collected in fractions by passing through the solution, and fractions with high specific activity were collected.

After dilution so that the conductivity was 10 ms or less, it was passed through a blue sepharose column. Transglutaminase was adsorbed by this operation. Furthermore, 005M phosphate buffer (pH
After washing away impure proteins in step 7), a salt concentration range of 0 to IM was created and a solution was passed through the tube to recover the eluate, and both fractions with high specific activity were collected. Concentrate using UF 6000 membrane to 0. 5M
Equilibration was carried out using a 0.05 M phosphate buffer (pH 7) containing 100 ml of sodium chloride.

{11 The f, l fi solution obtained was passed through a column containing Hif7dex G-75 (manufactured by Pharmacia Fine Chemicals) that had been equilibrated in advance with the same buffer solution, and the same slow leopard solution was passed through it to fractionate the eluate. did. As a result, the active fraction was eluted as a single peak. The specific activity of this product was 625 times that of the culture filtrate, and the recovery rate was 47%.

b) Production of BTG-2 In the same manner as in the case of BTG-1, Strebtoverticillium griseoluneum I FO 12776 was added to 3
After culturing at 0°C for 3 days, filter the culture, and transfer 19 liters of the culture solution to 17.

The activity of this product was 0.28 u/d.

The enzyme was purified in the same manner as for BTG-1, and the SD
Koichi's enzyme was obtained by S-disk electrophoresis.

c) Manufacture of B-cho G-3 In the same manner as in the case of B-cho G-1, Streptoverticillium sinanaeum sub-S. , culture medium 18. 5 I got 1. The enzyme activity of this product is 0.
It was 5u/d.

Purify the soybean in the same manner as in the case of BTG-1 and obtain SD
Koichi's enzyme was obtained by S-disk electrophoresis.

The present invention will be further explained below with reference to Examples.

Example 1 Raw material Booz (9 months aged Tudor cheese with water added,
Milk solids content was adjusted to 403%, milk protein was adjusted to 1.115.8%, and melted salt LJCHA-89. Phosphate mixture made by Hoechst Japan) was added to the raw cheese at 25% by weight, 8
The mixture was heated and stirred at 0°C.

After that, the temperature was lowered to 50°C and the melted cheese was treated with transglutaminase BTG-1 (specific activity 2.95LJ/η).
was dissolved in water and mixed to give an activity of 11 u/g protein, followed by reaction with stirring at 50°C for 30 minutes.

The reaction was stopped by sterilization treatment at 85° C. for 30 minutes, and the mixture was cooled to obtain a cheese food product.

For comparison, a cheese hood was prepared in exactly the same way except that transglutaminapi was not used (
control).

100 g of the obtained product was collected in a beaker, and the temperature of the product was measured in a hot water bath while the condition of the threads was visually examined. As a result, the cheese food of the present invention clearly shows stringiness. The lower limit of the temperature of the product was 50°C and the upper limit was 72°C, whereas the control cheese food did not exhibit any stringiness. In terms of meltdown properties, the cheese food of the present invention was refreshing and very smooth, whereas the control cheese food showed rapid melting properties, but did not melt excessively due to strong heating. This resulted in a significant decrease in viscosity.

Examples 2 to 14 In these Examples, cheese foods were manufactured according to the cheese food manufacturing method described in Example 1. Important manufacturing conditions and physical properties of the obtained products are shown in Table 1. I'll post all together.

The products obtained in these Examples were also examined for meltdown property (easily melted) and stringability in the same manner as described in Example 1, and both were found to be good.

In addition, Examples 4.5, 7, 8.10 and 11 are examples in which casein was added as a desired additive.

Table Example 15 Raw cheese (9-month aged, 1-dark cheese) was added with water to adjust the milk solids content to 40.3% and the Japanese horseradish protein content to 158%. ω%
After the addition, the mixture was heated and melted at 80°C.

Thereafter, the melted cheese was cooled at 50°C and transferred to transglutaminase BTG-1 (specific activity 2.95u/my).
> was added and mixed so as to increase the activity of i5LJ/9 protein, which was filled and molded into a container, and enzymatic reaction was performed at the same temperature for 2 hours.

Thereafter, the reaction was stopped by sterilization treatment at 85° C. for 30 minutes, and the mixture was cooled to obtain a cheese food product.

For comparison, a cheese food was produced in exactly the same manner except that transglutaminase was not used (control).

1g of the product was cut into cubes of 30mm on each side, 10 pieces were heated in a beaker with hot water (80℃, 30 minutes), and the other 10 pieces were heated in an oven on filter paper (180℃, 15 minutes). The spread unevenness and heat resistance and shape retention were investigated. As a result, the cheese food of the present invention did not show any spread on the bottom surface and had good shape retention, whereas the control cheese food suffered from melting and oil separation.

In addition, regarding the structure, the cheese food of the present invention had a pumpkin-like or hamben-like structure, and did not separate or sag. Regarding the freezing resistance, the structure after freezing was the same as that of the non-frozen one. On the other hand, the control cheese food caused water separation and became frozen water that adhered to the surface of the cheese.

Examples 16 to 20 In these Examples, cheese foods were manufactured according to the cheese food manufacturing method described in Example 15, and important rTIJ manufacturing conditions and physical properties of the products were implemented. They are summarized in Table 2 along with those of Example 15.

Regarding the products listed in 11I in these examples,
When the heat resistance and preservation properties were examined in the same manner as described in Example 15, it was found to have elastic and good shape preservation properties.

Example 17 is an example in which desired additives were added for comparison with casein and cheese.

It is shown in Table 3.

In addition, in Table 2, A in the evaluation of heat-resistant shape retention is -1 under heating conditions of 30 minutes at 80°C and 15 minutes at 180°C.
It is a rank that has shape retention in minutes, and the evaluation grade A in terms of freezing resistance is a rank that shows good tissue condition after being stored at -80°C for 3 days.

Claims (1)

[Claims] (1) Transglutaminase is made to act on a melted cheese having a milk solid content of 35% by weight or more and a milk protein content of 13% by weight or more, which is prepared by melting natural cheese or processed cheese by adding water and molten salt. A method for producing a cheese food that is easily meltable and stringy or has heat-resistant shape retention properties.